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Database: UniProt
Entry: A0A1F8M9W2_9CHLR
LinkDB: A0A1F8M9W2_9CHLR
Original site: A0A1F8M9W2_9CHLR 
ID   A0A1F8M9W2_9CHLR        Unreviewed;       349 AA.
AC   A0A1F8M9W2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OGN95399.1};
GN   ORFNames=A2Z77_03975 {ECO:0000313|EMBL:OGN95399.1};
OS   Chloroflexi bacterium RBG_13_51_36.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797625 {ECO:0000313|EMBL:OGN95399.1, ECO:0000313|Proteomes:UP000179678};
RN   [1] {ECO:0000313|EMBL:OGN95399.1, ECO:0000313|Proteomes:UP000179678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGN95399.1}.
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DR   EMBL; MGMS01000055; OGN95399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8M9W2; -.
DR   STRING; 1797625.A2Z77_03975; -.
DR   Proteomes; UP000179678; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          5..289
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   349 AA;  37386 MW;  0A34517AD7F76DCF CRC64;
     MKVIDLRSDT VTHPTPEMRK AMFEAEVGDD VYREDPTVNR LEAMAAMMMG KDAALFTTSG
     TQGNLIAVLA QTHHGNEIIV GDEAHMLWYE VGGAAALGGV TMRTVPNDSC GRLNLDDVER
     IIRTKDVHYP ETTLLCLENT HNRCGGMVLT AAYTDEVCSL AHTHGLKVHL DGARIFNAAV
     AQGVKASALA KNVDSVALCL SKGLGAPVGS LLCGSENLVG RARKFRKMLG GGMRQAGVIA
     AAGIVALETM VERLAEDHAN AKRLAQGLAD IKGITLAQDD VPTNIVMFEL APELSVGKFM
     RGLEEAGVKV GLRDTRPFRA VTHWMVSSSD IDEALVCIDT VCRKLHCPA
//
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